HEADER LYASE 10-APR-09 3H0W
TITLE HUMAN ADOMETDC WITH 5'-DEOXY-5'-[(N-DIMETHYL)AMINO]-8-METHYL-ADENOSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: RESIDUES 1-67;
COMPND 5 SYNONYM: ADOMETDC, SAMDC, S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA
COMPND 6 CHAIN, S-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN;
COMPND 7 EC: 4.1.1.50;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: RESIDUES 69-334;
COMPND 13 SYNONYM: ADOMETDC, SAMDC, S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA
COMPND 14 CHAIN, S-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN;
COMPND 15 EC: 4.1.1.50;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AMD1, AMD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: AMD1, AMD;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ADOMETDC WITH COMPETITIVE SUBSTRATE ANALOGS, AUTOCATALYTIC CLEAVAGE,
KEYWDS 2 DECARBOXYLASE, LYASE, PHOSPHOPROTEIN, POLYAMINE BIOSYNTHESIS,
KEYWDS 3 PYRUVATE, S-ADENOSYL-L-METHIONINE, SCHIFF BASE, SPERMIDINE
KEYWDS 4 BIOSYNTHESIS, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BALE,W.H.BROOKS,J.W.HANES,A.M.MAHESAN,W.C.GUIDA,S.E.EALICK
REVDAT 6 15-NOV-23 3H0W 1 LINK ATOM
REVDAT 5 06-SEP-23 3H0W 1 REMARK LINK
REVDAT 4 01-NOV-17 3H0W 1 REMARK
REVDAT 3 01-DEC-09 3H0W 1 AUTHOR
REVDAT 2 21-JUL-09 3H0W 1 JRNL
REVDAT 1 30-JUN-09 3H0W 0
JRNL AUTH S.BALE,W.BROOKS,J.W.HANES,A.M.MAHESAN,W.C.GUIDA,S.E.EALICK
JRNL TITL ROLE OF THE SULFONIUM CENTER IN DETERMINING THE LIGAND
JRNL TITL 2 SPECIFICITY OF HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 48 6423 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19527050
JRNL DOI 10.1021/BI900590M
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 127036.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 28205
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1387
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3386
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 176
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2429
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.68000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : -9.61000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 31.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN.PARAM
REMARK 3 PARAMETER FILE 2 : PYRUVOYL.PARAM
REMARK 3 PARAMETER FILE 3 : NMM.PARAM
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PYRUVOYL.TOP
REMARK 3 TOPOLOGY FILE 3 : NMM.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3H0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052551.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28205
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7150
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
REMARK 200 R SYM FOR SHELL (I) : 0.21500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1I7B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8000, 100 MM TRIS, 10 MM DTT,
REMARK 280 PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.72450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.50950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.72450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.50950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 352 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 433 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 ASP B 24
REMARK 465 ALA B 25
REMARK 465 ASN B 26
REMARK 465 PRO A 165
REMARK 465 GLU A 166
REMARK 465 SER A 167
REMARK 465 ARG A 168
REMARK 465 VAL A 169
REMARK 465 ILE A 170
REMARK 465 SER A 171
REMARK 465 GLN A 172
REMARK 465 PRO A 173
REMARK 465 GLN A 288
REMARK 465 SER A 289
REMARK 465 SER A 290
REMARK 465 LYS A 291
REMARK 465 CYS A 292
REMARK 465 ARG A 293
REMARK 465 THR A 294
REMARK 465 VAL A 295
REMARK 465 LEU A 296
REMARK 465 ALA A 297
REMARK 465 SER A 298
REMARK 465 PRO A 299
REMARK 465 LYS A 328
REMARK 465 GLN A 329
REMARK 465 GLN A 330
REMARK 465 GLN A 331
REMARK 465 GLN A 332
REMARK 465 GLN A 333
REMARK 465 SER A 334
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN B 21 -75.34 -54.83
REMARK 500 GLN B 22 -36.75 140.40
REMARK 500 GLN B 48 46.70 73.91
REMARK 500 CYS A 82 -155.02 -132.84
REMARK 500 LEU A 86 70.24 -105.22
REMARK 500 PRO A 126 30.39 -95.76
REMARK 500 SER A 154 -140.17 -147.32
REMARK 500 PHE A 250 43.68 -154.79
REMARK 500 ILE A 302 106.37 59.31
REMARK 500 PHE A 315 -125.49 -88.31
REMARK 500 ASN A 316 -84.81 -68.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N8M A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUT B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 68
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JEN RELATED DB: PDB
REMARK 900 RELATED ID: 1I7B RELATED DB: PDB
REMARK 900 RELATED ID: 1I72 RELATED DB: PDB
REMARK 900 RELATED ID: 1I7M RELATED DB: PDB
REMARK 900 RELATED ID: 1I79 RELATED DB: PDB
REMARK 900 RELATED ID: 1I7C RELATED DB: PDB
REMARK 900 RELATED ID: 3H0V RELATED DB: PDB
DBREF 3H0W B 1 67 UNP P17707 DCAM_HUMAN 1 67
DBREF 3H0W A 69 334 UNP P17707 DCAM_HUMAN 69 334
SEQRES 1 B 67 MET GLU ALA ALA HIS PHE PHE GLU GLY THR GLU LYS LEU
SEQRES 2 B 67 LEU GLU VAL TRP PHE SER ARG GLN GLN PRO ASP ALA ASN
SEQRES 3 B 67 GLN GLY SER GLY ASP LEU ARG THR ILE PRO ARG SER GLU
SEQRES 4 B 67 TRP ASP ILE LEU LEU LYS ASP VAL GLN CYS SER ILE ILE
SEQRES 5 B 67 SER VAL THR LYS THR ASP LYS GLN GLU ALA TYR VAL LEU
SEQRES 6 B 67 SER GLU
SEQRES 1 A 266 SER MET PHE VAL SER LYS ARG ARG PHE ILE LEU LYS THR
SEQRES 2 A 266 CYS GLY THR THR LEU LEU LEU LYS ALA LEU VAL PRO LEU
SEQRES 3 A 266 LEU LYS LEU ALA ARG ASP TYR SER GLY PHE ASP SER ILE
SEQRES 4 A 266 GLN SER PHE PHE TYR SER ARG LYS ASN PHE MET LYS PRO
SEQRES 5 A 266 SER HIS GLN GLY TYR PRO HIS ARG ASN PHE GLN GLU GLU
SEQRES 6 A 266 ILE GLU PHE LEU ASN ALA ILE PHE PRO ASN GLY ALA ALA
SEQRES 7 A 266 TYR CYS MET GLY ARG MET ASN SER ASP CYS TRP TYR LEU
SEQRES 8 A 266 TYR THR LEU ASP PHE PRO GLU SER ARG VAL ILE SER GLN
SEQRES 9 A 266 PRO ASP GLN THR LEU GLU ILE LEU MET SER GLU LEU ASP
SEQRES 10 A 266 PRO ALA VAL MET ASP GLN PHE TYR MET LYS ASP GLY VAL
SEQRES 11 A 266 THR ALA LYS ASP VAL THR ARG GLU SER GLY ILE ARG ASP
SEQRES 12 A 266 LEU ILE PRO GLY SER VAL ILE ASP ALA THR MET PHE ASN
SEQRES 13 A 266 PRO CYS GLY TYR SER MET ASN GLY MET LYS SER ASP GLY
SEQRES 14 A 266 THR TYR TRP THR ILE HIS ILE THR PRO GLU PRO GLU PHE
SEQRES 15 A 266 SER TYR VAL SER PHE GLU THR ASN LEU SER GLN THR SER
SEQRES 16 A 266 TYR ASP ASP LEU ILE ARG LYS VAL VAL GLU VAL PHE LYS
SEQRES 17 A 266 PRO GLY LYS PHE VAL THR THR LEU PHE VAL ASN GLN SER
SEQRES 18 A 266 SER LYS CYS ARG THR VAL LEU ALA SER PRO GLN LYS ILE
SEQRES 19 A 266 GLU GLY PHE LYS ARG LEU ASP CYS GLN SER ALA MET PHE
SEQRES 20 A 266 ASN ASP TYR ASN PHE VAL PHE THR SER PHE ALA LYS LYS
SEQRES 21 A 266 GLN GLN GLN GLN GLN SER
HET PUT B 350 6
HET N8M A 368 22
HET PYR A 68 5
HETNAM PUT 1,4-DIAMINOBUTANE
HETNAM N8M 5'-DEOXY-5'-(DIMETHYLAMINO)-8-METHYLADENOSINE
HETNAM PYR PYRUVIC ACID
HETSYN PUT PUTRESCINE
FORMUL 3 PUT C4 H12 N2
FORMUL 4 N8M C13 H20 N6 O3
FORMUL 5 PYR C3 H4 O3
FORMUL 6 HOH *220(H2 O)
HELIX 1 1 ASP B 31 ILE B 35 5 5
HELIX 2 2 PRO B 36 GLN B 48 1 13
HELIX 3 3 LEU A 86 LYS A 89 5 4
HELIX 4 4 ALA A 90 TYR A 101 1 12
HELIX 5 5 LYS A 119 GLN A 123 5 5
HELIX 6 6 ASN A 129 ALA A 139 1 11
HELIX 7 7 ASP A 185 ASP A 190 1 6
HELIX 8 8 GLN A 191 TYR A 193 5 3
HELIX 9 9 THR A 199 SER A 207 1 9
HELIX 10 10 ILE A 209 ILE A 213 5 5
HELIX 11 11 GLU A 247 PHE A 250 5 4
HELIX 12 12 TYR A 264 LYS A 276 1 13
SHEET 1 A 8 SER B 50 LYS B 56 0
SHEET 2 A 8 GLN B 60 SER B 66 -1 O ALA B 62 N THR B 55
SHEET 3 A 8 MET A 70 SER A 73 -1 O VAL A 72 N GLU B 61
SHEET 4 A 8 ARG A 76 THR A 81 -1 O ARG A 76 N SER A 73
SHEET 5 A 8 LYS B 12 SER B 19 -1 N LYS B 12 O THR A 81
SHEET 6 A 8 SER A 106 LYS A 115 -1 O SER A 113 N LEU B 13
SHEET 7 A 8 CYS A 156 LEU A 162 -1 O TYR A 158 N ARG A 114
SHEET 8 A 8 GLY A 144 GLY A 150 -1 N MET A 149 O TRP A 157
SHEET 1 B 8 VAL A 217 MET A 222 0
SHEET 2 B 8 TYR A 228 MET A 233 -1 O SER A 229 N THR A 221
SHEET 3 B 8 TYR A 239 THR A 245 -1 O ILE A 244 N TYR A 228
SHEET 4 B 8 TYR A 252 THR A 257 -1 O TYR A 252 N THR A 245
SHEET 5 B 8 GLN A 175 SER A 182 -1 N MET A 181 O VAL A 253
SHEET 6 B 8 LYS A 279 VAL A 286 -1 O LYS A 279 N SER A 182
SHEET 7 B 8 ASN A 319 ALA A 326 -1 O PHE A 325 N PHE A 280
SHEET 8 B 8 LYS A 306 MET A 314 -1 N GLN A 311 O PHE A 322
LINK C PYR A 68 N SER A 69 1555 1555 1.53
CISPEP 1 TYR A 125 PRO A 126 0 0.02
CISPEP 2 ASN A 224 PRO A 225 0 0.35
SITE 1 AC1 15 CYS A 82 PHE A 223 ASN A 224 CYS A 226
SITE 2 AC1 15 GLY A 227 TYR A 228 SER A 229 ILE A 244
SITE 3 AC1 15 THR A 245 PRO A 246 GLU A 247 HOH A 383
SITE 4 AC1 15 PHE B 7 SER B 66 GLU B 67
SITE 1 AC2 8 HOH A 11 PHE A 111 ASP A 174 THR A 176
SITE 2 AC2 8 PHE A 285 LEU B 13 GLU B 15 HOH B 80
SITE 1 AC3 7 SER A 69 LYS A 80 THR A 81 HIS A 243
SITE 2 AC3 7 HOH A 374 VAL B 64 LEU B 65
CRYST1 99.449 51.019 68.692 90.00 105.32 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010055 0.000000 0.002754 0.00000
SCALE2 0.000000 0.019601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015094 0.00000
(ATOM LINES ARE NOT SHOWN.)
END